The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.
Secreted Phospholipase A2-X Human Recombinant is manufactured with N-terminal fusion HisTag. PLA2G10 His-Tagged Fusion Protein, is 15.5 kDa containing 123 amino acid residues of the human secreted phospholipase A2-X and 16 additional amino acid residues - HisTag (underlined).
PLA2G10 filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 20mM Tris and 50mM NaCl, pH 7.5.
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino acid sequence
MRGSHHHHHH GMASHMGILE LAGTVGCVGP RTPIAYMKYG CFCGLGGHGQ PRDAIDWCCH GHDCCYTRAE EAGCSPKTER YSWQCVNQSV LCGPAENKCQ ELLCKCDQEI ANCLAQTEYN LKYLFYPQFL CEPDSPKCD